Author
Listed:
- Klaus van Leyen
(Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center)
- Robert M. Duvoisin
(Dyson Vision Research Institute, Cornell University Medical College
Cornell University Graduate School of Medical Sciences)
- Harald Engelhardt
(Max-Planck-Institut für Biochemie)
- Martin Wiedmann
(Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center
Cornell University Graduate School of Medical Sciences)
Abstract
Membrane-enclosed organelles, a defining characteristic of eukaryotic cells, are lost during differentiation of specific cell types such as reticulocytes (an intermediate in differentiation of erythrocytes), central fibre cells the eye lens, and keratinocytes1. The degradation of these organelles must be tightly regulated with respect to both the time of activation and the specificity of membrane degradation. The expression of 15-lipoxygenase (15-LOX) peaks in reticulocytes immediately before organelle degradation2. Here we show that 15-LOX integrates into the membranes of various organelles, allowing release of proteins from the organelle lumen and access of proteases to both lumenal and integral membrane proteins. In addition, by sparing the plasma membrane, 15-LOX shows the required specificity for organellar membranes. Thus, the action of 15-LOX provides a mechanism by which the natural degradation process can be explained. This conclusion is supported by our finding that lipoxygenase expression in the eye lens is restricted to the region at which organelle degradation occurs.
Suggested Citation
Klaus van Leyen & Robert M. Duvoisin & Harald Engelhardt & Martin Wiedmann, 1998.
"A function for lipoxygenase in programmed organelle degradation,"
Nature, Nature, vol. 395(6700), pages 392-395, September.
Handle:
RePEc:nat:nature:v:395:y:1998:i:6700:d:10.1038_26500
DOI: 10.1038/26500
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